Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein
| Autor: | John T. M. Kennis, Ivo H. M. van Stokkum, Klaas J. Hellingwerf, Marie Louise Groot, Jos C. Arents, Enis Arik, Jörn Weißenborn, Patrick E. Konold |
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| Přispěvatelé: | LaserLaB - Energy, Biophysics Photosynthesis/Energy, LaserLaB - Biophotonics and Microscopy, Biophotonics and Medical Imaging, Amsterdam Neuroscience - Brain Imaging |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Reaction kinetics and dynamics Materials science Light Protein Conformation Science Kinetics General Physics and Astronomy Model system 02 engineering and technology Crystal structure Crystallography X-Ray Photoreceptors Microbial Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Bacterial Proteins Ultrafast laser spectroscopy lcsh:Science X-ray crystallography Photoactive yellow protein Multidisciplinary Molecular Structure Spectrum Analysis Proteins General Chemistry Molecular conformation Photochemical Processes 021001 nanoscience & nanotechnology 030104 developmental biology Chemical physics Femtosecond lcsh:Q Absorption (chemistry) 0210 nano-technology |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020) Nature Communications Nature Communications, 11(1):4248, 1-12. Nature Publishing Group Konold, P E, Arik, E, Weißenborn, J, Arents, J C, Hellingwerf, K J, van Stokkum, I H M, Kennis, J T M & Groot, M L 2020, ' Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein ', Nature Communications, vol. 11, no. 1, 4248, pp. 1-12 . https://doi.org/10.1038/s41467-020-18065-9 |
| ISSN: | 2041-1723 |
| Popis: | Femtosecond time-resolved crystallography (TRC) on proteins enables resolving the spatial structure of short-lived photocycle intermediates. An open question is whether confinement and lower hydration of the proteins in the crystalline state affect the light-induced structural transformations. Here, we measured the full photocycle dynamics of a signal transduction protein often used as model system in TRC, Photoactive Yellow Protein (PYP), in the crystalline state and compared those to the dynamics in solution, utilizing electronic and vibrational transient absorption measurements from 100 fs over 12 decades in time. We find that the photocycle kinetics and structural dynamics of PYP in the crystalline form deviate from those in solution from the very first steps following photon absorption. This illustrates that ultrafast TRC results cannot be uncritically extrapolated to in vivo function, and that comparative spectroscopic experiments on proteins in crystalline and solution states can help identify structural intermediates under native conditions. Protein structural dynamics can be studied by time-resolved crystallography (TRC) and ultrafast transient spectroscopic methods. Here, the authors perform electronic and vibrational transient absorption measurements to characterise the full photocycle of Photoactive Yellow Protein (PYP) both in the crystalline and solution state and find that the photocycle kinetics and structural intermediates of PYP deviate in the crystalline state, which must be taken into consideration when planning TRC experiments. |
| Databáze: | OpenAIRE |
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